ID A0A0D9X4K0_9ORYZ Unreviewed; 1837 AA.
AC A0A0D9X4K0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR08G03360.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR08G03360.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR08G03360.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR08G03360.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU004279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00024550,
CC ECO:0000256|RuleBase:RU004279};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR STRING; 77586.A0A0D9X4K0; -.
DR EnsemblPlants; LPERR08G03360.1; LPERR08G03360.1; LPERR08G03360.
DR Gramene; LPERR08G03360.1; LPERR08G03360.1; LPERR08G03360.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR Proteomes; UP000032180; Chromosome 8.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 2.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 12.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 9.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 242..548
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1543..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 694..721
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1566..1656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1837 AA; 205267 MW; C522EB0BF3FF98AC CRC64;
MDARFPYSPA EVSKVELVQF GILSPDEIRQ MSVVMIEHAE TMERGKPKPG GLSDPRLGTI
DRKIKCETCM AGMAECPGHF GHLELAKPMF HIGFIKTVLS IMRCVCFNCS KILADEEDTK
FKQALKIRNP KNRLKRIYDA CKSKKVCAGG DDLEVQDQQD TDEPVKKRGG CGAQQPNITV
DGMKMVAEFK AAKKKNDDQE QLPEPVERKQ ILSAERVLNV LKRISDEDCL LLGLNPKFAR
PDWMILQVLP IPPPPVRPSV MMDTSSRSED DLTHQLAMII RHNENLRRQE RNGAPAHIIT
EFAQLLQFHI ATYFDNELPG QPRATQRSGR PIKSICSRLK AKEGRIRGNL MGKRVDFSAR
TVITPDPNIN IDELGVPWSI ALNLTYPETV TPYNIERLKE LVEYGPHPPP GKTGAKYIIR
EDGQRLDLRY VKKSSDQHLE LGYKVERHLN DGDFVLFNRQ PSLHKMSIMG HRIKIMPYST
FRLNLSVTSP YNADFDGDEM NMHVPQSFET RAEVLELMMV PKCIVSPQSN RPVMGIVQDT
LLGCRKITKR DTLIEKDVFM NILMWWEDFD GKVPAPAILK PRPIWTGKQV FNLIIPKQIN
LIRFSAWHSE TETGFITPGD TVVRIEKGEL LSGTLCKKTL GTGTGSLIHV IWEEVGPDAA
RKFLGHTQWL VNYWLLQNGF SIGIGDTIAD ASTMEKINET ISKAKNDVKE LIKQAHDKQL
EAEPGRTMME SFENRVNQVL NKARDDAGSS AQKSLSESNN LKAMVTAGSK GSFINISQMT
ACVGQQNVEG KRIPFGFVDR TLPHFTKDDY GPESRGFVEN SYLRGLTPQE FFFHAMGGRE
GLIDTAVKTS ETGYIQRRLV KAMEDIMVKY DGTVRNSLGD VIQFLYGEDG MDAVWIESQK
LDSLKMKKAE FDNVFRYELD DENWRPNYML PDHVDDLKTI REFRNVFEAE VQKLEGDRLQ
LGTEIATTGD NTWPMPVNLK RLIWNAQKTF KIDLRRPSDM HPMEIVEAID KLQERLKVVP
GDDAMSIEAQ KNATLFFNIL LRSTFASKRV LKEYRLTKEA FEWVIGEIES RFLQSLVAPG
EMIGCVAAQS IGEPATQMTL NTFHYAGVSA KNVTLGVPRL REIINVAKKI KTPSLSVYLK
PEVNKKKELA KNVQCALEYT TLRSVTHATE IWYDPDPLGT IIEEDVEFVR SYYEMPDEDI
DPDKISPWLL RIELNREMMV DKKLSMADIA EKINHEFDDD LSCIFNDDNA DKLILRVRIT
NDEAPKGEIQ DESAEDDVFL KKIESNMLTE MALRGIPDIN KVFIKYGKVN KFEDNDGFKS
EQEWMLDTEG VNLLAVMCHE DVDATRTTSN HLIEVIEVLG IEAVRRALLD ELRVVISFDG
SYVNYRHLAI LCDTMTYRGH LMAITRHGIN RNDTGPLMRC SFEETVDILL DAAVYAESDY
LRGVTENIML GQLAPIGTGG CALYLNDQML QQAIELQLPS YVESLDFGMT PARSPISGTP
YHEGMMSPST YLLSPNIRAS PITDAQFSPY VGGMAFSPVP SPGYTPSSGG GYSPSSPVYS
PGPGGGYSPT SPSYSPASPS YSPTSPSYTP GSPTYSPTSP SYSPTSPSYS PTSPSYSPTS
PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPPNFT CIQPNISILQ PHITVIQPNI
APNISIIQSD VSLIQPHLPF LQSNITLIQP NIACIQPYFS WVQPDITKLQ PNFAKLQSNL
AKLQSFFGQV QSFTCVLSNP TSPTYSPTSP SYSQPSPSYS PTSPYTTSGG PSPDYSPTSP
NYSPSGSYSP TAPGYSLSST GQQFSPKAGD KDDENAQ
//
